4gvq
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_4gvq| PDB=4gvq | SCENE= }} | {{STRUCTURE_4gvq| PDB=4gvq | SCENE= }} | ||
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===X-ray structure of the Archaeoglobus fulgidus methenyl-tetrahydromethanopterin cyclohydrolase in complex with tetrahydromethanpterin=== | ===X-ray structure of the Archaeoglobus fulgidus methenyl-tetrahydromethanopterin cyclohydrolase in complex with tetrahydromethanpterin=== | ||
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{{ABSTRACT_PUBMED_23013430}} | {{ABSTRACT_PUBMED_23013430}} | ||
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+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/MCH_ARCFU MCH_ARCFU]] Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT. | ||
==About this Structure== | ==About this Structure== | ||
- | [[4gvq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4gvq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GVQ OCA]. |
- | [[Category: | + | |
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:023013430</ref><references group="xtra"/><references/> | ||
+ | [[Category: Arcfu]] | ||
[[Category: Methenyltetrahydromethanopterin cyclohydrolase]] | [[Category: Methenyltetrahydromethanopterin cyclohydrolase]] | ||
[[Category: Demmer, U.]] | [[Category: Demmer, U.]] |
Revision as of 07:58, 5 February 2014
Contents |
X-ray structure of the Archaeoglobus fulgidus methenyl-tetrahydromethanopterin cyclohydrolase in complex with tetrahydromethanpterin
Template:ABSTRACT PUBMED 23013430
Function
[MCH_ARCFU] Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
About this Structure
4gvq is a 3 chain structure with sequence from Arcfu. Full crystallographic information is available from OCA.
Reference
- Upadhyay V, Demmer U, Warkentin E, Moll J, Shima S, Ermler U. Structure and catalytic mechanism of N(5),N(10)-methenyl-tetrahydromethanopterin cyclohydrolase. Biochemistry. 2012 Oct 23;51(42):8435-43. doi: 10.1021/bi300777k. Epub 2012 Oct, 8. PMID:23013430 doi:http://dx.doi.org/10.1021/bi300777k